9 research outputs found
PKC-dependent phosphorylation of the p97 repressor regulates the transcription of aldolase A L-type promoter
Expression of mouse aldolase A L-type mRNA is negatively modulated by a cis element (AldA-NRE), located within the aldolase A distal promoter (pL). AldA-NRE interacts with a 97-kDa repressor protein (p97), which binds DNA in a cell cycle-dependent manner. We demonstrate that the binding between AldA-NRE and p97 decreases during differentiation of human Caco-2 cells and is inversely correlated with L-type mRNA expression. Phosphorylation of the p97 repressor weakened its DNA binding activity in differentiated Caco-2 cells, while dephosphorylation enhanced the binding in proliferating cells. Stimulation of protein kinase C (PKC) in vivo decreased the binding of p97 to AldA-NRE and stimulated transcription, while inhibition of PKC stimulated p97 binding and downregulated transcription. These findings suggest that PKC is a mediator of the binding and silencing function of the p97/AldA-NRE repressor complex. Copyright (C) 1999 Federation of European Biochemical Societies
Transcription of aldolase a l-type promoter is regulated by a pkc dependent phosphorylation of a p97 repressor.
PKC-dependent phosphorylation of the p97 repressor regulates the transcription of aldolase A L-type promoter
A RARE CASE OF COMPOUND HETEROZYGOSITY FOR DELTA+27 AND HB NEAPOLIS (DHONBURI) ASSOCIATED TO AN ATYPICAL BETA-THALASEMIA PHENOTYPE
A rare case of compound heterozygosity for d+ thalassemia and Hb Neapolis (Dhonburi) associated with an atypical b-thalassemia phenotype.
A rare case of compound heterozygosity for d+ thalassemia and Hb Neapolis (Dhonburi) associated with an atypical b-thalassemia phenotype.
A RARE CASE OF COMPOUND HETEROZYGOSITY FOR DELTA+27 AND HB NEAPOLIS (DHONBURI) ASSOCIATED TO AN ATYPICAL BETA-THALASEMIA PHENOTYPE
PKC-dependent phosphorylation of the p97 repressor regulates the transcription of aldolase A L-type promoter
AbstractExpression of mouse aldolase A L-type mRNA is negatively modulated by a cis element (AldA-NRE), located within the aldolase A distal promoter (pL). AldA-NRE interacts with a 97-kDa repressor protein (p97), which binds DNA in a cell cycle-dependent manner. We demonstrate that the binding between AldA-NRE and p97 decreases during differentiation of human Caco-2 cells and is inversely correlated with L-type mRNA expression. Phosphorylation of the p97 repressor weakened its DNA binding activity in differentiated Caco-2 cells, while dephosphorylation enhanced the binding in proliferating cells. Stimulation of protein kinase C (PKC) in vivo decreased the binding of p97 to AldA-NRE and stimulated transcription, while inhibition of PKC stimulated p97 binding and downregulated transcription. These findings suggest that PKC is a mediator of the binding and silencing function of the p97/AldA-NRE repressor complex
